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Volumn 44, Issue 51, 2005, Pages 16844-16852

Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYST ACTIVITY; ENZYMES; ESCHERICHIA COLI; MOLECULES; MUTAGENESIS;

EID: 29344456431     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051681j     Document Type: Article
Times cited : (19)

References (16)
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  • 3
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  • 4
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    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L., and Koonin, E. V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches, J. Mol. Biol. 287, 1023.
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    • Aravind, L.1    Koonin, E.V.2
  • 8
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    • Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis
    • Cho, Y., Sharma, V., and Sacchettini, J. C. (2003) Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis, J. Biol. Chem. 278, 8333-8339.
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  • 10
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    • Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase
    • Grant, G. A., Hu, Z., and Xu, X. L. (2003) Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase, J. Biol. Chem. 278, 18170-18176.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18170-18176
    • Grant, G.A.1    Hu, Z.2    Xu, X.L.3
  • 11
    • 1842741352 scopus 로고    scopus 로고
    • Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers
    • Grant, G. A., Xu, X. L., and Hu, Z. (2004) Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers, J. Biol. Chem. 279, 13452-13460.
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  • 12
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    • Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase
    • Thompson, J. R., Bell, J. K., Bratt, J., Grant, G. A., and Banaszak, L. J. (2005) Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase, Biochemistry 44, 5763-5773.
    • (2005) Biochemistry , vol.44 , pp. 5763-5773
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  • 13
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    • The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding
    • Al-Rabiee, R., Lee, E. J., and Grant, G. A. (1996) The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding, J. Biol. Chem. 271, 13013-13017.
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  • 14
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    • Inverse thinking about double mutant enzymes
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  • 15
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    • Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects
    • Grant, G. A., Xu, X. L., and Hu, Z. (2000) Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects, Arch. Biochem. Biophys. 375, 171-174.
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  • 16
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    • Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase
    • Grant, G. A., Xu, X. L., and Hu, Z. (2000) Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase, Biochemistry 39, 7316-7319.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.